Proteomic and computational characterisation of 11S globulins from grape seed flour by-product and its interaction with malvidin 3-glucoside by molecular docking

•Grape seed flour residue is proposed as new protein source of industrial interest.•Globulin from grape seed flour were studied by proteomic and computational tools.•Two 11S globulins of grape seed V. vinifera L were identified by MALDI-TOF/TOF.•3D structure of 11S globulins were theoretically elucidated for the first time.•Molecular Docking suggests 11S globulins-mv3glc interactions like 7S globulins. Grape seed flour by-product (GSBP) is an economic and renewable source of proteins, increasingly being explored due to interesting technological application such as colour protection in rich-anthocyanins beverages. Globulin-like proteins from GSBP were characterised by proteomic and computational studies. MALDI TOF/TOF analysis revealed the presence of two 11S globulins (acid and basic), whose 3D structures have been elucidated for the first time in Vitis vinifera L. grape seeds by using homology models and molecular dynamics. The secondary structure showed 11 α-helices and 25 β-sheets for acid and 12 α-helices and 24 β-sheets for basic 11S globulins. Molecular docking results indicate that both grape seed 11S globulins could establish different types of non-covalent interactions (π-π) with malvidin 3-O-glucoside (wine anthocyanin), which suggest a possible colour protection similar to that occurring in copigmentation phenomenon. These findings provide valuable information of globulin family proteins that could be relevant in food industry applications.